Nucleic acid binding properties of the nucleic acid chaperone domain of hepatitis delta antigen

Chun Chung Wang, Tsung Cheng Chang, Ching Wen Lin, Hsiu Ling Tsui, Page B C Chu, Bo Shun Chen, Zhi Shun Huang, Huey Nan Wu

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

The N terminal region of hepatitis delta antigen (HDAg), referred to here as NdAg, has a nucleic acid chaperone activity that modulates the ribozyme activity of hepatitis delta virus (HDV) RNA and stimulates hammerhead ribozyme catalysis. We characterized the nucleic acid binding properties of NdAg, identified the structural and sequence domains important for nucleic acid binding, and studied the correlation between the nucleic acid binding ability and the nucleic acid chaperone activity. NdAg does not recognize the catalytic core of HDV ribozyme specifically. Instead, NdAg interacts with a variety of nucleic acids and has higher affinities to longer nucleic acids. The studies with RNA homopolymers reveal that the binding site size of NdAg is around nine nucleotides long. The extreme N terminal portion of NdAg, the following coiled-coil domain and the basic amino acid clusters in these regions are important for nucleic acid binding. The nucleic acid-NdAg complex is stabilized largely by electrostatic interactions. The formation of RNA-protein complex appears to be a prerequisite for facilitating hammerhead ribozyme catalysis of NdAg and its derivatives. Mutations that reduce the RNA binding activity or high ionic strength that destabilizes the RNA-protein complex, reduce the nucleic acid chaperone activity of NdAg.

Original languageEnglish (US)
Pages (from-to)6481-6492
Number of pages12
JournalNucleic acids research
Volume31
Issue number22
DOIs
StatePublished - Nov 15 2003

ASJC Scopus subject areas

  • Genetics

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